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Volumn 170, Issue 1, 2005, Pages 47-59

α-synuclein targets the plasma membrane via the secretory pathway and induces toxicity in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; PROTEASOME;

EID: 20444372698     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: 10.1534/genetics.104.035493     Document Type: Article
Times cited : (102)

References (64)
  • 1
    • 0037115490 scopus 로고    scopus 로고
    • Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function
    • BABU, P., J. D. BRYAN, H. R. PANEK, S. L. JORDAN, B. M. FORBRICH et al., 2002 Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function. J. Cell Sci. 115: 4957-4968.
    • (2002) J. Cell Sci. , vol.115 , pp. 4957-4968
    • Babu, P.1    Bryan, J.D.2    Panek, H.R.3    Jordan, S.L.4    Forbrich, B.M.5
  • 2
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • BANKAITIS, V. A., D. E. MALEHORN, S. D. EMR and R. GREENE, 1989 The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J. Cell Biol. 108: 1271-1281.
    • (1989) J. Cell Biol. , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 3
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • BARLOWE, C., L. ORCI, T. YEUNG, M. HOSOBUCHI, S. HAMAMOTO et al., 1994 COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77: 895-907.
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1    Orci, L.2    Yeung, T.3    Hosobuchi, M.4    Hamamoto, S.5
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • BENCE, N. F., R. M. SAMPAT and R. R. KOPITO, 2001 Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 5
    • 0038689039 scopus 로고    scopus 로고
    • Protein aggregation and the ubiquitin proteasome pathway: Gaining the UPPer hand on neurodegeneration
    • BERKE, S. J., and H. L. PAULSON, 2003 Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration. Curr. Opin. Genet. Dev. 13: 253-261.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 253-261
    • Berke, S.J.1    Paulson, H.L.2
  • 8
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • BRENNWALD, P., B. KEARNS, K. CHAMPION, S. KERANEN, V. BANKAITIS et al., 1994 Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79: 245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keranen, S.4    Bankaitis, V.5
  • 9
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins
    • BUSSELL, R., JR., and D. ELIEZER, 2003 A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329: 763-778.
    • (2003) J. Mol. Biol. , vol.329 , pp. 763-778
    • Bussell Jr., R.1    Eliezer, D.2
  • 10
    • 1942534598 scopus 로고    scopus 로고
    • Effects of Parkinson's disease-linked mutations on the structure of lipid-associated alpha-synuclein
    • BUSSELL, R., JR., and D. ELIEZER, 2004 Effects of Parkinson's disease-linked mutations on the structure of lipid-associated alpha-synuclein. Biochemistry 43: 4810-4818.
    • (2004) Biochemistry , vol.43 , pp. 4810-4818
    • Bussell Jr., R.1    Eliezer, D.2
  • 11
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • CABIN, D. E., K. SHIMAZU, D. MURPHY, N. B. COLE, W. GOTTSCHALK et al., 2002 Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J. Neurosci. 22: 8797-8807.
    • (2002) J. Neurosci. , vol.22 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5
  • 13
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein
    • COLE, N. B., D. D. MURPHY, T. GRIDER, S. RUETER, D. BRASAEMLE et al., 2002 Lipid droplet binding and oligomerization properties of the Parkinson's disease protein alpha-synuclein. J. Biol. Chem. 277: 6344-6352.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6344-6352
    • Cole, N.B.1    Murphy, D.D.2    Grider, T.3    Rueter, S.4    Brasaemle, D.5
  • 14
    • 0038199712 scopus 로고    scopus 로고
    • Overproduction of polypeptides corresponding to the amino terminus of the F-box proteins Cdc4p and Met30p inhibits ubiquitin ligase activities of their SCF complexes
    • DIXON, C., L. E. BRUNSON, M. M. ROY, D. SMOTHERS, M. G. SEHORN et al., 2003 Overproduction of polypeptides corresponding to the amino terminus of the F-box proteins Cdc4p and Met30p inhibits ubiquitin ligase activities of their SCF complexes. Eukaryot. Cell 2: 123-133.
    • (2003) Eukaryot. Cell , vol.2 , pp. 123-133
    • Dixon, C.1    Brunson, L.E.2    Roy, M.M.3    Smothers, D.4    Sehorn, M.G.5
  • 15
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • ELBLE, R., 1992 A simple and efficient procedure for transformation of yeasts. Biotechniques 13: 18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 16
    • 0037424263 scopus 로고    scopus 로고
    • Dynamic chromatin alterations triggered by natural and synthetic activation domains
    • ERKINE, A. M., and D. S. GROSS, 2003 Dynamic chromatin alterations triggered by natural and synthetic activation domains. J. Biol. Chem. 278: 7755-7764.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7755-7764
    • Erkine, A.M.1    Gross, D.S.2
  • 17
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • FEANY, M. B., and W. W. BENDER, 2000 A Drosophila model of Parkinson's disease. Nature 404: 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 18
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • FERRO-NOVICK, S., and R. JAHN, 1994 Vesicle fusion from yeast to man. Nature 370: 191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 19
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • GEORGE, J. M., H. JIN, W. S. WOODS and D. F. CLAYTON, 1995 Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron 15: 361-372.
    • (1995) Neuron , vol.15 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 20
    • 0030844524 scopus 로고    scopus 로고
    • Protein folding. The difference with prokaryotes
    • GETHING, M. J., 1997 Protein folding. The difference with prokaryotes. Nature 388: 329, 331.
    • (1997) Nature , vol.388 , pp. 329
    • Gething, M.J.1
  • 21
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • GOSAVI, N., H. J. LEE, J. S. LEE, S. PATEL and S. J. LEE, 2002 Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem. 277: 48984-48992.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 22
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • HEINEMEYER, W., J. A. KLEINSCHMIDT, J. SAIDOWSKY, C. ESCHER and D. H. WOLF, 1991 Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10: 555-562.
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 23
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins
    • HEINEMEYER, W., A. GRUHLER, V. MOHRLE, Y. MAHE and D. H. WOLF, 1993 PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268: 5115-5120.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Mohrle, V.3    Mahe, Y.4    Wolf, D.H.5
  • 24
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro
    • HOYER, W., D. CHERNY, V. SUBRAMANIAM and T. M. JOVIN, 2004 Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry 43: 16233-16242.
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 26
    • 0029820770 scopus 로고    scopus 로고
    • Characterization of the precursor protein of the non-A beta component of senile plaques (NACP) in the human central nervous system
    • IRIZARRY, M. C., T. W. KIM, M. MCNAMARA, R. E. TANZI, J. M. GEORGE et al., 1996 Characterization of the precursor protein of the non-A beta component of senile plaques (NACP) in the human central nervous system. J. Neuropathol. Exp. Neurol. 55: 889-895.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 889-895
    • Irizarry, M.C.1    Kim, T.W.2    Mcnamara, M.3    Tanzi, R.E.4    George, J.M.5
  • 27
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • JENNER, P., and C. W. OLANOW, 1998 Understanding cell death in Parkinson's disease. Ann. Neurol. 44: S72-S84.
    • (1998) Ann. Neurol. , vol.44
    • Jenner, P.1    Olanow, C.W.2
  • 28
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • JENSEN, P. H., M. S. NIELSEN, R. JAKES, C. G. DOTTI and M. GOEDERT, 1998 Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem. 273: 26292-26294.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 29
    • 0036307753 scopus 로고    scopus 로고
    • Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein
    • JO, E., N. FULLER, R. P. RAND, P. ST. GEORGE-HYSLOP and P. E. FRASER, 2002 Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein. J. Mol. Biol. 315: 799-807.
    • (2002) J. Mol. Biol. , vol.315 , pp. 799-807
    • Jo, E.1    Fuller, N.2    Rand, R.P.3    St. George-Hyslop, P.4    Fraser, P.E.5
  • 30
    • 0034280435 scopus 로고    scopus 로고
    • Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain
    • KAHLE, P. J., M. NEUMANN, L. OZMEN, V. MULLER, H. JACOBSEN et al., 2000 Subcellular localization of wild-type and Parkinson's disease-associated mutant alpha-synuclein in human and transgenic mouse brain. J. Neurosci. 20: 6365-6373.
    • (2000) J. Neurosci. , vol.20 , pp. 6365-6373
    • Kahle, P.J.1    Neumann, M.2    Ozmen, L.3    Muller, V.4    Jacobsen, H.5
  • 31
    • 0031588598 scopus 로고    scopus 로고
    • Evidence that the precursor protein of non-A beta component of Alzheimer's disease amyloid (NACP) has an extended structure primarily composed of random-coil
    • KIM, J., 1997 Evidence that the precursor protein of non-A beta component of Alzheimer's disease amyloid (NACP) has an extended structure primarily composed of random-coil. Mol. Cells 7: 78-83.
    • (1997) Mol. Cells , vol.7 , pp. 78-83
    • Kim, J.1
  • 32
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • KITADA, T., S. ASAKAWA, N. HATTORI, H. MATSUMINE, Y. YAMAMURA et al., 1998 Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5
  • 33
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • KROBITSCH, S., and S. LINDQUIST, 2000 Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl. Acad. Sci. USA 97: 1589-1594.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 34
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • KRUGER, R., W. KUHN, T. MULLER, D. WOITALLA, M. GRAEBER et al., 1998 Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat. Genet. 18: 106-108.
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5
  • 35
    • 0033549568 scopus 로고    scopus 로고
    • Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9
    • LEHMAN, K., G. ROSSI, J. E. ADAMO and P. BRENNWALD, 1999 Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J. Cell Biol. 146: 125-140.
    • (1999) J. Cell Biol. , vol.146 , pp. 125-140
    • Lehman, K.1    Rossi, G.2    Adamo, J.E.3    Brennwald, P.4
  • 36
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by alpha-synuclein filaments and oligomers
    • LINDERSSON, E., R. BEEDHOLM, P. HOJRUP, T. MOOS, W. GAI et al., 2004 Proteasomal inhibition by alpha-synuclein filaments and oligomers. J. Biol. Chem. 279: 12924-12934.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3    Moos, T.4    Gai, W.5
  • 37
    • 0030728226 scopus 로고    scopus 로고
    • Mad cows meet psi-chotic yeast: The expansion of the prion hypothesis
    • LINDQUIST, S., 1997 Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89: 495-498.
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 38
    • 0034489853 scopus 로고    scopus 로고
    • Alpha-synuclein and Parkinson's disease
    • LUCKING, C. B., and A. BRICE, 2000 Alpha-synuclein and Parkinson's disease. Cell. Mol. Life Sci. 57: 1894-1908.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1894-1908
    • Lucking, C.B.1    Brice, A.2
  • 39
    • 0023722437 scopus 로고
    • Synuclein: A neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • MAROTEAUX, L., J. T. CAMPANELLI and R. H. SCHELLER, 1988 Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8: 2804-2815.
    • (1988) J. Neurosci. , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 40
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • MASLIAH, E., E. ROCKENSTEIN, I. VEINBERGS, M. MALLORY, M. HASHIMOTO et al., 2000 Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 287: 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5
  • 41
    • 0034979314 scopus 로고    scopus 로고
    • Lack of nigral pathology in transgenic mice expressing human alpha-synuclein driven by the tyrosine hydroxylase promoter
    • MATSUOKA, Y., M. VILA, S. LINCOLN, A. MCCORMACK, M. PICCIANO et al., 2001 Lack of nigral pathology in transgenic mice expressing human alpha-synuclein driven by the tyrosine hydroxylase promoter. Neurobiol. Dis. 8: 535-539.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 535-539
    • Matsuoka, Y.1    Vila, M.2    Lincoln, S.3    Mccormack, A.4    Picciano, M.5
  • 42
    • 0024325454 scopus 로고
    • Basal-level expression of the yeast HSP82 gene requires a heat shock regulatory element
    • MCDANIEL, D., A. J. CAPLAN, M. S. LEE, C. C. ADAMS, B. R. FISHEL et al., 1989 Basal-level expression of the yeast HSP82 gene requires a heat shock regulatory element. Mol. Cell. Biol. 9: 4789-4798.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4789-4798
    • Mcdaniel, D.1    Caplan, A.J.2    Lee, M.S.3    Adams, C.C.4    Fishel, B.R.5
  • 43
    • 0034708767 scopus 로고    scopus 로고
    • Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations
    • MCLEAN, P. J., H. KAWAMATA, S. RIBICH and B. T. HYMAN, 2000 Membrane association and protein conformation of alpha-synuclein in intact neurons. Effect of Parkinson's disease-linked mutations. J. Biol. Chem. 275: 8812-8816.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8812-8816
    • Mclean, P.J.1    Kawamata, H.2    Ribich, S.3    Hyman, B.T.4
  • 44
    • 0037036904 scopus 로고    scopus 로고
    • Proteasome inhibition causes nigral degeneration with inclusion bodies in rats
    • MCNAUGHT, K. S., L. M. BJORKLUND, R. BELIZAIRE, O. ISACSON, P. JENNER et al., 2002 Proteasome inhibition causes nigral degeneration with inclusion bodies in rats. Neuroreport 13: 1437-1441.
    • (2002) Neuroreport , vol.13 , pp. 1437-1441
    • Mcnaught, K.S.1    Bjorklund, L.M.2    Belizaire, R.3    Isacson, O.4    Jenner, P.5
  • 45
    • 0027182508 scopus 로고
    • Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast
    • MITCHELL, D. A., T. K. MARSHALL and R. J. DESCHENES, 1993 Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast 9: 715-722.
    • (1993) Yeast , vol.9 , pp. 715-722
    • Mitchell, D.A.1    Marshall, T.K.2    Deschenes, R.J.3
  • 46
    • 0036938142 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactiviry in normal and neoplastic Schwann cells
    • MORI, F., C. INENAGA, M. YOSHIMOTO, H. UMEZU, R. TANAKA et al., 2002 Alpha-synuclein immunoreactiviry in normal and neoplastic Schwann cells. Acta Neuropathol. 103: 145-151.
    • (2002) Acta Neuropathol. , vol.103 , pp. 145-151
    • Mori, F.1    Inenaga, C.2    Yoshimoto, M.3    Umezu, H.4    Tanaka, R.5
  • 47
    • 0033018150 scopus 로고    scopus 로고
    • A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum
    • NISHIMURA, N., S. BANNYKH, S. SLABOUGH, J. MATTESON, Y. ALTSCHULER et al., 1999 A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum. J. Biol. Chem. 274: 15937-15946.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15937-15946
    • Nishimura, N.1    Bannykh, S.2    Slabough, S.3    Matteson, J.4    Altschuler, Y.5
  • 49
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • NOVICK, P., C. FIELD and R. SCHEKMAN, 1980 Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21: 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 50
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into alpha-synuclein biology and pathobiology
    • OUTEIRO, T. F., and S. LINDQUIST, 2003 Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science 302: 1772-1775.
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 51
    • 0032199167 scopus 로고    scopus 로고
    • Autosomal dominant Parkinson's disease
    • POLYMEROPOULOS, M. H., 1998 Autosomal dominant Parkinson's disease. J. Neurol. 245: 1-3.
    • (1998) J. Neurol. , vol.245 , pp. 1-3
    • Polymeropoulos, M.H.1
  • 52
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • POLYMEROPOULOS, M. H., C. LAVEDAN, E. LEROY, S. E. IDE, A. DEHEJIA et al., 1997 Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276: 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 53
    • 0033916138 scopus 로고    scopus 로고
    • The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsfl in vivo and is required for the induction of heat shock genes by oxidative stress
    • RAITT, D. C., A. L. JOHNSON, A. M. ERKINE, K. MAKINO, B. MORGAN et al., 2000 The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsfl in vivo and is required for the induction of heat shock genes by oxidative stress. Mol. Biol. Cell 11: 2335-2347.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2335-2347
    • Raitt, D.C.1    Johnson, A.L.2    Erkine, A.M.3    Makino, K.4    Morgan, B.5
  • 54
    • 4344641972 scopus 로고    scopus 로고
    • Interactions among alpha-synuclein, dopamine, and biomembranes: Some clues for understanding neurodegeneration in Parkinson's disease
    • ROCHET, J. C., T. F. OUTEIRO, K. A. CONWAY, T. T. DING, M. J. VOLLES et al., 2004 Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. J. Mol. Neurosci. 23: 23-34.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 23-34
    • Rochet, J.C.1    Outeiro, T.F.2    Conway, K.A.3    Ding, T.T.4    Volles, M.J.5
  • 55
    • 0003529272 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • ROSE, M. D., F. WINSTON and P. HIETER, 1990 A Laboratory Course. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1990) A Laboratory Course
    • Rose, M.D.1    Winston, F.2    Hieter, P.3
  • 56
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • ROTHMAN, J. E., 1994 Mechanisms of intracellular protein transport. Nature 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 57
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: Implications for Parkinson's disease
    • SHIMURA, H., M. G. SCHLOSSMACHER, N. HATTORI, M. P. FROSCH, A. TROCKENBACHER et al., 2001 Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293: 263-269.
    • (2001) Science , vol.293 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5
  • 58
    • 0242300619 scopus 로고    scopus 로고
    • alpha-Synuclein locus triplication causes Parkinson's disease
    • SINGLETON, A. B., M. FARRER, J. JOHNSON, A. SINGLETON, S. HAGUE et al., 2003 alpha-Synuclein locus triplication causes Parkinson's disease. Science 302: 841.
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3    Singleton, A.4    Hague, S.5
  • 60
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins
    • SYME, C. D., E. W. BLANCH, C. HOLT, R. JAKES, M. GOEDERT et al., 2002 A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins. Eur. J. Biochem. 269: 148-156.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5
  • 61
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • TANAKA, Y., S. ENGELENDER, S. IGARASHI, R. K. RAO, T. WANNER et al., 2001 Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum. Mol. Genet. 10: 919-926.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5
  • 62
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • TAYLOR, J. P., J. HARDY and K. H. FISCHBECK, 2002 Toxic proteins in neurodegenerative disease. Science 296: 1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 64
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • WEINREB, P. H., W. ZHEN, A. W. POON, K. A. CONWAY and P. T. LANSBURY, JR., 1996 NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35: 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5


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